##gff-version 3
Q9GZQ8	UniProtKB	Chain	1	120	.	.	.	ID=PRO_0000017198;Note=Microtubule-associated proteins 1A/1B light chain 3B	
Q9GZQ8	UniProtKB	Propeptide	121	125	.	.	.	ID=PRO_0000017199;Note=Removed in mature form	
Q9GZQ8	UniProtKB	Site	120	121	.	.	.	Note=Cleavage%3B by ATG4B;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355958;Dbxref=PMID:15355958	
Q9GZQ8	UniProtKB	Lipidation	120	120	.	.	.	Note=Phosphatidylethanolamine amidated glycine%3B alternate;Ontology_term=ECO:0000269,ECO:0000305,ECO:0000305;evidence=ECO:0000269|PubMed:33909989,ECO:0000305|PubMed:15187094,ECO:0000305|PubMed:29458288;Dbxref=PMID:15187094,PMID:29458288,PMID:33909989	
Q9GZQ8	UniProtKB	Lipidation	120	120	.	.	.	Note=Phosphatidylserine amidated glycine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33909989;Dbxref=PMID:33909989	
Q9GZQ8	UniProtKB	Mutagenesis	26	26	.	.	.	Note=Increased interaction with WDFY3/ALFY%2C no effect on SQSTM1-binding%3B when associated with Y-27 and D-57. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24668264;Dbxref=PMID:24668264	
Q9GZQ8	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Decreased interaction with Legionella effector RavZ. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28668392;Dbxref=PMID:28668392	
Q9GZQ8	UniProtKB	Mutagenesis	27	27	.	.	.	Note=Increased interaction with WDFY3/ALFY%2C no effect on SQSTM1-binding%3B when associated with K-26 and D-57. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24668264;Dbxref=PMID:24668264	
Q9GZQ8	UniProtKB	Mutagenesis	35	35	.	.	.	Note=Decreases C18 ceramide binding. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22922758;Dbxref=PMID:22922758	
Q9GZQ8	UniProtKB	Mutagenesis	52	53	.	.	.	Note=No effect on interaction with TECPR2. FL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20562859;Dbxref=PMID:20562859	
Q9GZQ8	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Decreases C18 ceramide binding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22922758;Dbxref=PMID:22922758	
Q9GZQ8	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Increased interaction with WDFY3/ALFY%2C no effect on SQSTM1-binding%3B when associated with K-26 and Y-27. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24668264;Dbxref=PMID:24668264	
Q9GZQ8	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Impairs cleavage by ATG4B. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23721406;Dbxref=PMID:23721406	
Q9GZQ8	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Abolishes interaction with TECPR2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20562859;Dbxref=PMID:20562859	
Q9GZQ8	UniProtKB	Mutagenesis	80	82	.	.	.	Note=Impaired localization to autophagosomes. FLL->ALA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31315929;Dbxref=PMID:31315929	
Q9GZQ8	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Abolished delipidation by ATG4 family proteins. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31315929;Dbxref=PMID:31315929	
Q9GZQ8	UniProtKB	Mutagenesis	119	119	.	.	.	Note=Impaired localization to autophagosomes. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31315929;Dbxref=PMID:31315929	
Q9GZQ8	UniProtKB	Mutagenesis	120	120	.	.	.	Note=No processing of precursor. No lipidation. Decreases C18 ceramide binding. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15355958,ECO:0000269|PubMed:22922758;Dbxref=PMID:15355958,PMID:22922758	
Q9GZQ8	UniProtKB	Mutagenesis	122	122	.	.	.	Note=No effect on processing of precursor. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355958;Dbxref=PMID:15355958	
Q9GZQ8	UniProtKB	Sequence conflict	61	61	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9GZQ8	UniProtKB	Helix	2	4	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3X0W	
Q9GZQ8	UniProtKB	Helix	7	10	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Helix	13	26	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Beta strand	30	37	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Beta strand	42	44	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3VTW	
Q9GZQ8	UniProtKB	Beta strand	51	55	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Helix	60	71	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Beta strand	75	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5DCN	
Q9GZQ8	UniProtKB	Beta strand	80	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Turn	84	86	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Turn	89	91	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3VTU	
Q9GZQ8	UniProtKB	Beta strand	92	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MS5	
Q9GZQ8	UniProtKB	Helix	95	102	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Beta strand	105	107	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W9A	
Q9GZQ8	UniProtKB	Beta strand	109	114	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN	
Q9GZQ8	UniProtKB	Helix	116	124	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6LAN